未经证实:蜘蛛毒液通过与分子靶标高亲和力结合而诱导不同的生理药理作用,因此具有生物技术意义。其中一些毒素,作用于不同类型的离子通道,已经在Phoneutria属蜘蛛的毒液中发现,主要来自P.Nigriventer.尽管P.nigriventer毒素证明了药物潜力,关于同一属毒液分子的信息有限,因为它们的毒素特征仍然很差。了解这种多样性并阐明蜘蛛毒素作用机制的差异对于建立其真正的生物技术潜力至关重要。这促使我们比较了Phoneutria属的三种不同毒液:P.nigriventer(Pn-V),P.eickstedtae(Pe-V)和P.pertyi(Pp-V)。
UNASSIGNED:通过SDS-PAGE对毒液进行生化和功能比较,HPLC,质谱,酶活性和电生理测定(全细胞膜片钳)。
未经评估:所采用的方法表明,所有三种毒液在其成分上都具有整体相似性,只有微小的差异。大量类似蛋白质的存在是显而易见的,特别是质量范围为~6.0kDa的毒素。在所有毒液中均检测到透明质酸酶和蛋白水解活性,除了毒素Tx1和Tx2-6的同种型。所有Tx1同工型都阻断了Nav1.6离子电流,略有不同。
未经批准:我们的研究结果表明,Pn-V,Pe-V和Pp-V在蛋白质组成和酶活性方面非常相似,含有具有高度序列同源性的相同毒素的同种型,小修改。然而,这些结构和功能的变化对毒液的多样性非常重要。此外,我们的发现将有助于理解Phoneutria属其他物种毒液的分子多样性,暴露其生物技术潜力作为寻找新活性分子的来源。
UNASSIGNED: Spider venoms induce different physio-pharmacological effects by binding with high affinity on molecular targets, therefore being of biotechnological interest. Some of these toxins, acting on different types of ion channels, have been identified in the venom of spiders of the genus
Phoneutria, mainly from P. nigriventer. In spite of the pharmaceutical potential demonstrated by P. nigriventer toxins, there is limited information on molecules from venoms of the same genus, as their toxins remain poorly characterized. Understanding this diversity and clarifying the differences in the mechanisms of action of spider toxins is of great importance for establishing their true biotechnological potential. This prompted us to compare three different venoms of the
Phoneutria genus: P. nigriventer (Pn-V), P. eickstedtae (Pe-V) and P. pertyi (Pp-V).
UNASSIGNED: Biochemical and functional comparison of the venoms were carried out by SDS-PAGE, HPLC, mass spectrometry, enzymatic activities and electrophysiological assays (whole-cell patch clamp).
UNASSIGNED: The employed approach revealed that all three venoms had an overall similarity in their components, with only minor differences. The presence of a high number of similar proteins was evident, particularly toxins in the mass range of ~6.0 kDa. Hyaluronidase and proteolytic activities were detected in all venoms, in addition to isoforms of the toxins Tx1 and Tx2-6. All Tx1 isoforms blocked Nav1.6 ion currents, with slight differences.
UNASSIGNED: Our findings showed that Pn-V, Pe-V and Pp-V are highly similar concerning protein composition and enzymatic activities, containing isoforms of the same toxins sharing high sequence homology, with minor modifications. However, these structural and functional variations are very important for venom diversity. In addition, our findings will contribute to the comprehension of the molecular diversity of the venoms of the other species from
Phoneutria genus, exposing their biotechnological potential as a source for searching for new active molecules.